کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5512481 | 1540225 | 2017 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Comprehensive analysis of α 2-3-linked sialic acid specific Maackia amurensis leukagglutinin reveals differentially occupied N-glycans and C-terminal processing
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Seeds of Maackia amurensis constitutes two sialic acid specific agglutinins known as leukagglutinin and hemagglutinin. Maackia amurensis leukagglutinin (MAL) recognizes α2-3-linked sialic acid present mainly in N-glycans and composed of two disulfide linked monomers. It exhibits potential N-glycosylation sites (four PNGs) which have been assumed to undergo differential occupancy. In this study we have characterized the site specific macro- and microheterogeneity of monomers in detail by analysing N-glycopeptides and peptides through liquid chromatography coupled to ion trap mass spectrometer in MS3 mode (LC-MSn). We observed the presence of mainly paucimannose N-glycans at Asn61, Asn113 and Asn191 whereas a high mannose type with varying Man5-9 occurs at Asn179. Interestingly Asn179 and Asn191 exhibited differential occupancy which was evident by the presence of non-glycosylated peptides. This has contributed to the difference in molecular mass of monomers upon SDS-PAGE. Further the presence of disulfide linked peptides confirmed the covalent linkage of monomers which also undergoes uniform C-terminal processing.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 94, Part A, January 2017, Pages 114-121
Journal: International Journal of Biological Macromolecules - Volume 94, Part A, January 2017, Pages 114-121
نویسندگان
Gnanesh Kumar B.S, Avadhesha Surolia,